CH60_PSEPU
ID CH60_PSEPU Reviewed; 545 AA.
AC P48216; Q9R5K4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WCS358;
RX PubMed=7845355; DOI=10.1007/bf00279758;
RA Venturi V., Wolfs K., Leong J., Weisbeek P.J.;
RT "Amplification of the groESL operon in Pseudomonas putida increases
RT siderophore gene promoter activity.";
RL Mol. Gen. Genet. 245:126-132(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-17.
RC STRAIN=PHE39.34;
RX PubMed=1352616; DOI=10.1111/j.1365-2958.1992.tb00880.x;
RA Fowell S.L., Lilley K.S., Jones D., Maxwell A.;
RT "GroEL proteins from three Pseudomonas species.";
RL Mol. Microbiol. 6:1575-1576(1992).
CC -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential
CC role in assisting protein folding. The GroEL-GroES system forms a nano-
CC cage that allows encapsulation of the non-native substrate proteins and
CC provides a physical environment optimized to promote and accelerate
CC protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00600};
CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC rings stacked back-to-back. Interacts with the co-chaperonin GroES.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; X78435; CAA55199.1; -; Genomic_DNA.
DR PIR; S51563; S51563.
DR AlphaFoldDB; P48216; -.
DR SMR; P48216; -.
DR STRING; 1240350.AMZE01000055_gene514; -.
DR PRIDE; P48216; -.
DR eggNOG; COG0459; Bacteria.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Isomerase;
KW Nucleotide-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1352616"
FT CHAIN 2..545
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063487"
FT BINDING 30..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 87..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 477..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
SQ SEQUENCE 545 AA; 56304 MW; 5766377486957A2E CRC64;
MAAKDVKFGD SARKKMLVGV NVLADAVKAT LGPKGRNVVL AKSFGAPTIT KDGVSVAKEI
ELKDAFENMG AQLVKEVASK ANDAAGDGTT TATVLAQSIV NEGLKAVAAG MNPMDLKRGI
DKATAAVVAE LKNLSKPCAD SKAIAQVGTI SANSDSSIGE IIAEAMEKVG KEGVITVEEG
SGLENELSVV EGMQFDRGYL SPYFVNKPDT MVAELEGPLL LLVDKKISTS RAAASTERAS
AGRPLLIVAE DVEGEALATL VVNNMRGIVK VAAVKAPGFG DRRKAMLQDI AVLTGGQVIS
EEIGVSLETA TLEHLGNAKR VILSKENTTI IDGAGADTEI EARVKQIRAQ IEETSSDYDR
EKLQERLAKL AGGVAVIKVG AGTEVEMKEK KARVEDALHA TRAAVEEGVV PGGGVALVRA
LNAIVDLKGD NEDQNVGIAL LRRAVESPLR QITANAGDEP SVVANKVKQG SGNFGYNAAT
GEYGDMIEMG ILDPAKVTRS ALQAAASIGG LMITTEAMIA DAPSDAPAGG GMPDMGGMGG
MGGMM
